메뉴 건너뛰기




Volumn 84, Issue 6, 2014, Pages 605-620

Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in endoplasmic reticulum derived organelles

Author keywords

Cell wall degradation; Developmental tissue remodeling; ER bodies; Programmed cell death; Ricinosomes

Indexed keywords

ARABIDOPSIS; RICINUS COMMUNIS;

EID: 84896044639     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11103-013-0157-6     Document Type: Article
Times cited : (22)

References (56)
  • 1
    • 0030931105 scopus 로고    scopus 로고
    • Proteinase A, a storage-globulin-degrading endopeptidase of vetch (Vicia sativa L.) seeds, is not involved in early steps of storage protein mobilization
    • doi:10.1111/j.1432-1033.1997.00304.x
    • Becker C, Senyuk VI, Shutov AD, Nong VH, Fischer J, Horstmann C, Müntz K (1997) Proteinase A, a storage-globulin-degrading endopeptidase of vetch (Vicia sativa L.) seeds, is not involved in early steps of storage protein mobilization. Eur J Biochem 248: 304-312. doi: 10. 1111/j. 1432-1033. 1997. 00304. x.
    • (1997) Eur J Biochem , vol.248 , pp. 304-312
    • Becker, C.1    Senyuk, V.I.2    Shutov, A.D.3    Nong, V.H.4    Fischer, J.5    Horstmann, C.6    Müntz, K.7
  • 2
    • 0001193725 scopus 로고    scopus 로고
    • Programmed cell death during plant growth and development
    • Beers EP (1997) Programmed cell death during plant growth and development. Cell Death Differ 4: 649-661.
    • (1997) Cell Death Differ , vol.4 , pp. 649-661
    • Beers, E.P.1
  • 3
    • 0034476852 scopus 로고    scopus 로고
    • Plant proteolytic enzymes: possible role during programmed cell death
    • Beers EP, Woffenden BJ, Zhao C (2000) Plant proteolytic enzymes: possible role during programmed cell death. Plant Mol Biol 44: 399-415.
    • (2000) Plant Mol Biol , vol.44 , pp. 399-415
    • Beers, E.P.1    Woffenden, B.J.2    Zhao, C.3
  • 4
    • 0742322084 scopus 로고    scopus 로고
    • The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis
    • Beers EP, Jones AM, Dickerman AW (2004) The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis. Phytochemistry 65: 43-58.
    • (2004) Phytochemistry , vol.65 , pp. 43-58
    • Beers, E.P.1    Jones, A.M.2    Dickerman, A.W.3
  • 5
    • 0032519739 scopus 로고    scopus 로고
    • Stomata patterning on the hypocotyl of Arabidopsis thaliana is controlled by genes involved in the control of root epidermis patterning
    • Berger F, Linstead P, Dolan L, Haseloff J (1998) Stomata patterning on the hypocotyl of Arabidopsis thaliana is controlled by genes involved in the control of root epidermis patterning. Dev Biol 194: 226-234.
    • (1998) Dev Biol , vol.194 , pp. 226-234
    • Berger, F.1    Linstead, P.2    Dolan, L.3    Haseloff, J.4
  • 7
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins
    • doi:10.1105/tpc.104.027078
    • Carter C, Pan S, Zoihar J, Avila EL, Girke T, Raikhel NV (2004) The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell 16: 3285-3303. doi: 10. 1105/tpc. 104. 027078.
    • (2004) Plant Cell , vol.16 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zoihar, J.3    Avila, E.L.4    Girke, T.5    Raikhel, N.V.6
  • 8
    • 0033117455 scopus 로고    scopus 로고
    • Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea
    • Cercos M, Santamaria S, Carbonell JSO (1999) Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea. Plant Physiol 119: 1341-1348.
    • (1999) Plant Physiol , vol.119 , pp. 1341-1348
    • Cercos, M.1    Santamaria, S.2    Carbonell, J.S.O.3
  • 9
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • doi:10.1046/j.1365-313x.1998.00343.x
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743. doi: 10. 1046/j. 1365-313x. 1998. 00343. x.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 11
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at high frequency
    • doi:10.1073/pnas.97.7.3718
    • Cutler SR, Ehrhardt DW, Griffitts JS, Somerville CR (2000) Random GFP: cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at high frequency. Proc Natl Acad Sci USA 97: 3718-3723. doi: 10. 1073/pnas. 97. 7. 3718.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 12
    • 51749100088 scopus 로고    scopus 로고
    • Expression analysis of the BFN1 nuclease gene promoter during senescence, abscission, and programmed cell death-related processes
    • doi:10.1093/jxb/ern176
    • Farage-Barhom S, Burd S, Sonego L, Perl-Treves R, Lers A (2008) Expression analysis of the BFN1 nuclease gene promoter during senescence, abscission, and programmed cell death-related processes. J Exp Bot 59: 3247-3258. doi: 10. 1093/jxb/ern176.
    • (2008) J Exp Bot , vol.59 , pp. 3247-3258
    • Farage-Barhom, S.1    Burd, S.2    Sonego, L.3    Perl-Treves, R.4    Lers, A.5
  • 13
    • 82255194151 scopus 로고    scopus 로고
    • Localization of the Arabidopsis senescence- and cell death-associated BFN1 nuclease: from the ER to fragmented nuclei
    • doi:10.1093/mp/ssr045
    • Farage-Barhom S, Burd S, Sonego L, Mett A, Belausov E, Gidoni D, Lers A (2011) Localization of the Arabidopsis senescence- and cell death-associated BFN1 nuclease: from the ER to fragmented nuclei. Mol Plant 4: 1062-1073. doi: 10. 1093/mp/ssr045.
    • (2011) Mol Plant , vol.4 , pp. 1062-1073
    • Farage-Barhom, S.1    Burd, S.2    Sonego, L.3    Mett, A.4    Belausov, E.5    Gidoni, D.6    Lers, A.7
  • 14
    • 67649496487 scopus 로고    scopus 로고
    • Rapid combinatorial analysis of membrane compartments in intact plants with a multicolor marker set
    • doi:10.1111/j.1365-313X.2009.03851.x
    • Geldner N, Denervaud-Tendon V, Hyman DL, Mayer U, Stierhof Y-D, Chory J (2009) Rapid combinatorial analysis of membrane compartments in intact plants with a multicolor marker set. Plant J 59: 169-178. doi: 10. 1111/j. 1365-313X. 2009. 03851. x.
    • (2009) Plant J , vol.59 , pp. 169-178
    • Geldner, N.1    Denervaud-Tendon, V.2    Hyman, D.L.3    Mayer, U.4    Stierhof, Y.-D.5    Chory, J.6
  • 16
    • 0031105881 scopus 로고    scopus 로고
    • A cysteine endopeptidase isolated from castor bean endosperm microbodies processes the glyoxysomal malate dehydrogenase precursor protein
    • Gietl C, Wimmer B, Adamec J, Kalousek F (1997) A cysteine endopeptidase isolated from castor bean endosperm microbodies processes the glyoxysomal malate dehydrogenase precursor protein. Plant Physiol 113: 863-871.
    • (1997) Plant Physiol , vol.113 , pp. 863-871
    • Gietl, C.1    Wimmer, B.2    Adamec, J.3    Kalousek, F.4
  • 17
    • 13844312452 scopus 로고    scopus 로고
    • Ricinosomes and endosperm transfer cell structure in programmed cell death of the nucellus during Ricinus seed development
    • doi:10.1073/pnas.0409429102
    • Greenwood JS, Helm M, Gietl C (2005) Ricinosomes and endosperm transfer cell structure in programmed cell death of the nucellus during Ricinus seed development. Proc Natl Acad Sci USA 102: 2238-2243. doi: 10. 1073/pnas. 0409429102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2238-2243
    • Greenwood, J.S.1    Helm, M.2    Gietl, C.3
  • 18
  • 19
    • 79960228202 scopus 로고    scopus 로고
    • The role of vacuole in plant death
    • doi:10.1038/cdd.2011.70
    • Hara-Nishimura I, Hatsugai N (2011) The role of vacuole in plant death. Cell Death Differ 18: 1298-1304. doi: 10. 1038/cdd. 2011. 70.
    • (2011) Cell Death Differ , vol.18 , pp. 1298-1304
    • Hara-Nishimura, I.1    Hatsugai, N.2
  • 20
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein-storage vacuoles is mediated by large precursor-accumulating vesicles
    • doi:10.1105/tpc.10.5.825
    • Hara-Nishimura I, Shimada T, Hatano K, Takeuchim Y, Nishimura M (1998) Transport of storage proteins to protein-storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 10: 825-836. doi: 10. 1105/tpc. 10. 5. 825.
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchim, Y.4    Nishimura, M.5
  • 21
    • 16544378458 scopus 로고    scopus 로고
    • Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells
    • doi:10.1104/pp.104.053876
    • Hara-Nishimura I, Matsushima R, Shimada T, Nishimura M (2004) Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells. Plant Physiol 136: 3435-3439. doi: 10. 1104/pp. 104. 053876.
    • (2004) Plant Physiol , vol.136 , pp. 3435-3439
    • Hara-Nishimura, I.1    Matsushima, R.2    Shimada, T.3    Nishimura, M.4
  • 23
    • 0342803566 scopus 로고    scopus 로고
    • pGreen: a versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation
    • Hellens RP, Edwards EA, Leyland NR, Bean S, Mulineaux PM (2000) pGreen: a versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation. Plant Mol Biol 42: 819-832.
    • (2000) Plant Mol Biol , vol.42 , pp. 819-832
    • Hellens, R.P.1    Edwards, E.A.2    Leyland, N.R.3    Bean, S.4    Mulineaux, P.M.5
  • 24
    • 51349133279 scopus 로고    scopus 로고
    • KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells and dismantling of extensin scaffolds
    • doi:10.3732/ajb.2007404
    • Helm M, Schmid M, Hierl G, Terneus K, Tan L, Lottspeich F, Kieliszewski MJ, Gietl C (2008) KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells and dismantling of extensin scaffolds. Am J Bot 95: 1049-1062. doi: 10. 3732/ajb. 2007404.
    • (2008) Am J Bot , vol.95 , pp. 1049-1062
    • Helm, M.1    Schmid, M.2    Hierl, G.3    Terneus, K.4    Tan, L.5    Lottspeich, F.6    Kieliszewski, M.J.7    Gietl, C.8
  • 25
    • 0032718660 scopus 로고    scopus 로고
    • Protein storage bodies and vacuoles
    • doi:10.1105/tpc.11.4.601
    • Herman EM, Larkins BA (1999) Protein storage bodies and vacuoles. Plant Cell 11: 601-613. doi: 10. 1105/tpc. 11. 4. 601.
    • (1999) Plant Cell , vol.11 , pp. 601-613
    • Herman, E.M.1    Larkins, B.A.2
  • 26
    • 16544372267 scopus 로고    scopus 로고
    • Endoplasmatic reticulum to vacuole trafficking of endoplasmatic reticulum bodies an alternate pathway for protein transfer to the vacuole
    • doi:10.1104/pp.104.051722
    • Herman EM, Schmid M (2004) Endoplasmatic reticulum to vacuole trafficking of endoplasmatic reticulum bodies an alternate pathway for protein transfer to the vacuole. Plant Physiol 136: 3440-3446. doi: 10. 1104/pp. 104. 051722.
    • (2004) Plant Physiol , vol.136 , pp. 3440-3446
    • Herman, E.M.1    Schmid, M.2
  • 27
    • 84859848841 scopus 로고    scopus 로고
    • Programmed cell death in Ricinus and Arabidopsis: the function of KDEL cysteine peptidases in development
    • doi:10.1111/j.1399-3054.2012.01580.x
    • Hierl G, Vothknecht U, Gietl C (2012) Programmed cell death in Ricinus and Arabidopsis: the function of KDEL cysteine peptidases in development. Physiol Plant 145: 103-113. doi: 10. 1111/j. 1399-3054. 2012. 01580. x.
    • (2012) Physiol Plant , vol.145 , pp. 103-113
    • Hierl, G.1    Vothknecht, U.2    Gietl, C.3
  • 28
    • 0032066054 scopus 로고    scopus 로고
    • A common position-dependent mechanism controls cell-type patterning of GLABRA2 regulation in the root and hypocotyl epidermis of Arabidopsis
    • Hung CY, Lin Y, Zhang M, Pollock S, Marks MD, Schiefelbein J (1998) A common position-dependent mechanism controls cell-type patterning of GLABRA2 regulation in the root and hypocotyl epidermis of Arabidopsis. Plant Physiol 117: 73-84.
    • (1998) Plant Physiol , vol.117 , pp. 73-84
    • Hung, C.Y.1    Lin, Y.2    Zhang, M.3    Pollock, S.4    Marks, M.D.5    Schiefelbein, J.6
  • 29
    • 0034476827 scopus 로고    scopus 로고
    • Caspase-like protease involvement in the control of plant cell death
    • Lam E, delPozo O (2000) Caspase-like protease involvement in the control of plant cell death. Plant Mol Biol 44: 417-428.
    • (2000) Plant Mol Biol , vol.44 , pp. 417-428
    • Lam, E.1    delPozo, O.2
  • 30
    • 84864387731 scopus 로고    scopus 로고
    • Regulating the reapers: activating metacaspases for programmed cell death
    • Lam E, Zhang Y (2011) Regulating the reapers: activating metacaspases for programmed cell death. Trends Plant Sci 17: 487-494.
    • (2011) Trends Plant Sci , vol.17 , pp. 487-494
    • Lam, E.1    Zhang, Y.2
  • 31
    • 0346037065 scopus 로고    scopus 로고
    • An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis
    • Matsushima R, Hayashi Y, Shimada T, Nishimura M, Hara-Nishimura I (2002) An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis. Plant Physiol 130: 1807-1814.
    • (2002) Plant Physiol , vol.130 , pp. 1807-1814
    • Matsushima, R.1    Hayashi, Y.2    Shimada, T.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 32
    • 0242515793 scopus 로고    scopus 로고
    • A novel ER-derived compartment, the ER body, selectively accumulates ß-glucosidases with an ER-retention signal in Arabidopsis
    • doi:10.1046/j.1365-313X.2003.01636.x
    • Matsushima R, Kondo M, Nishimura M, Hara-Nishimura I (2003) A novel ER-derived compartment, the ER body, selectively accumulates ß-glucosidases with an ER-retention signal in Arabidopsis. Plant J 33: 493-502. doi: 10. 1046/j. 1365-313X. 2003. 01636. x.
    • (2003) Plant J , vol.33 , pp. 493-502
    • Matsushima, R.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 33
    • 0000528945 scopus 로고
    • Studies on seeds. V. Microbodies, glyoxysomes, and ricinosomes of castor bean endosperm
    • Mollenhauer HH, Totten C (1970) Studies on seeds. V. Microbodies, glyoxysomes, and ricinosomes of castor bean endosperm. Plant Physiol 46: 794-799.
    • (1970) Plant Physiol , vol.46 , pp. 794-799
    • Mollenhauer, H.H.1    Totten, C.2
  • 34
    • 34548406409 scopus 로고    scopus 로고
    • Protein dynamics and proteolysis in plant vacuoles
    • doi:10.1093/jxb/erm089
    • Müntz K (2007) Protein dynamics and proteolysis in plant vacuoles. J Exp Bot 58: 2391-2407. doi: 10. 1093/jxb/erm089.
    • (2007) J Exp Bot , vol.58 , pp. 2391-2407
    • Müntz, K.1
  • 35
    • 0019321718 scopus 로고
    • Rapid isolation of high-molecular-weight plant DNA
    • Murray MG, Thompson WF (1980) Rapid isolation of high-molecular-weight plant DNA. Nucleic Acids Res 8: 4321-4325.
    • (1980) Nucleic Acids Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 36
    • 0041464460 scopus 로고    scopus 로고
    • C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydryl-endopeptidase
    • doi:10.1104/pp.103.021147
    • Okamoto T, Shimada T, Hara-Nishimura I, Nishimura M, Minamikawa T (2003) C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydryl-endopeptidase. Plant Physiol 132: 1892-1900. doi: 10. 1104/pp. 103. 021147.
    • (2003) Plant Physiol , vol.132 , pp. 1892-1900
    • Okamoto, T.1    Shimada, T.2    Hara-Nishimura, I.3    Nishimura, M.4    Minamikawa, T.5
  • 37
    • 51349130209 scopus 로고    scopus 로고
    • Arabidopsis protein disulfide isomerase-5 inhibits cysteine protease during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds
    • doi:10.1105/tpc.108.058339
    • Ondzighi CA, Christopher DA, Cho EJ, Chang SC, Staehelin LA (2008) Arabidopsis protein disulfide isomerase-5 inhibits cysteine protease during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds. Plant Cell 20: 2205-2220. doi: 10. 1105/tpc. 108. 058339.
    • (2008) Plant Cell , vol.20 , pp. 2205-2220
    • Ondzighi, C.A.1    Christopher, D.A.2    Cho, E.J.3    Chang, S.C.4    Staehelin, L.A.5
  • 39
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • Schaller A (2004) A cut above the rest: the regulatory function of plant proteases. Planta 220: 183-197.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 40
    • 0032189507 scopus 로고    scopus 로고
    • A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment
    • Schmid M, Simpson D, Kalousek F, Gietl C (1998) A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment. Planta 206: 466-475.
    • (1998) Planta , vol.206 , pp. 466-475
    • Schmid, M.1    Simpson, D.2    Kalousek, F.3    Gietl, C.4
  • 41
    • 0033598774 scopus 로고    scopus 로고
    • Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes
    • doi:10.1073/pnas.96.24.14159
    • Schmid M, Simpson D, Gietl C (1999) Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes. Proc Natl Acad Sci USA 96: 14159-14164. doi: 10. 1073/pnas. 96. 24. 14159.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14159-14164
    • Schmid, M.1    Simpson, D.2    Gietl, C.3
  • 42
    • 0035942237 scopus 로고    scopus 로고
    • The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum
    • doi:10.1073/pnas.061038298
    • Schmid M, Simpson DJ, Sarioglu H, Lottspeich F, Gietl C (2001) The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Proc Natl Acad Sci USA 98: 5353-5358. doi: 10. 1073/pnas. 061038298.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5353-5358
    • Schmid, M.1    Simpson, D.J.2    Sarioglu, H.3    Lottspeich, F.4    Gietl, C.5
  • 43
    • 60249086952 scopus 로고    scopus 로고
    • Ricinosomes predict programmed cell death leading to anther dehiscence in tomato
    • doi:10.1104/pp.108.132720
    • Senatore A, Trobacher CP, Greenwood JS (2009) Ricinosomes predict programmed cell death leading to anther dehiscence in tomato. Plant Physiol 149: 775-790. doi: 10. 1104/pp. 108. 132720.
    • (2009) Plant Physiol , vol.149 , pp. 775-790
    • Senatore, A.1    Trobacher, C.P.2    Greenwood, J.S.3
  • 44
    • 0034773313 scopus 로고    scopus 로고
    • Proteolytic degradation of cereal prolamins-the problem with proline
    • Simpson DJ (2001) Proteolytic degradation of cereal prolamins-the problem with proline. Plant Sci 161: 825-838.
    • (2001) Plant Sci , vol.161 , pp. 825-838
    • Simpson, D.J.1
  • 45
    • 1242317042 scopus 로고    scopus 로고
    • The 2.0-Å crystal structure of the KDEL-tailed cysteine endopeptidase from germinating endosperm of Ricinus communis confirms its function in the final stage of programmed cell death
    • Than ME, Helm M, Simpson DJ, Lottspeich F, Huber R, Gietl C (2004) The 2. 0-Å crystal structure of the KDEL-tailed cysteine endopeptidase from germinating endosperm of Ricinus communis confirms its function in the final stage of programmed cell death. J Mol Biol 336: 1103-1116.
    • (2004) J Mol Biol , vol.336 , pp. 1103-1116
    • Than, M.E.1    Helm, M.2    Simpson, D.J.3    Lottspeich, F.4    Huber, R.5    Gietl, C.6
  • 46
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of a KDEL-tailed cysteine protease (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds
    • doi:10.1083/jcb.148.3.453
    • Toyooka K, Okamoto T, Minamikawa T (2000) Mass transport of a KDEL-tailed cysteine protease (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds. J Cell Biol 148: 453-463. doi: 10. 1083/jcb. 148. 3. 453.
    • (2000) J Cell Biol , vol.148 , pp. 453-463
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 47
    • 84874339107 scopus 로고    scopus 로고
    • Induction of a ricinosomal-protease and programmed cell death in tomato endosperm by gibberellic acid
    • Trobacher CP, Senatore A, Holley C, Greenwood JS (2013) Induction of a ricinosomal-protease and programmed cell death in tomato endosperm by gibberellic acid. Planta 237: 665-679.
    • (2013) Planta , vol.237 , pp. 665-679
    • Trobacher, C.P.1    Senatore, A.2    Holley, C.3    Greenwood, J.S.4
  • 50
    • 0014837856 scopus 로고
    • Cytochemical and developmental changes in microbodies (glyoxysomes) and related organelles of castor bean endosperm
    • Vigil EL (1970) Cytochemical and developmental changes in microbodies (glyoxysomes) and related organelles of castor bean endosperm. J Cell Biol 46: 435-454.
    • (1970) J Cell Biol , vol.46 , pp. 435-454
    • Vigil, E.L.1
  • 51
    • 34250886910 scopus 로고    scopus 로고
    • From analysis of mutants to genetic engineering
    • doi:10.1146/annurev.arplant.58.032806.104003
    • Von Wettstein D (2007) From analysis of mutants to genetic engineering. Ann Rev Plant Biol 58: 1-19. doi: 10. 1146/annurev. arplant. 58. 032806. 104003.
    • (2007) Ann Rev Plant Biol , vol.58 , pp. 1-19
    • Von Wettstein, D.1
  • 52
    • 70450181685 scopus 로고    scopus 로고
    • Plant caspase-like proteases in plant programmed cell death
    • Xu Q, Zhang L (2009) Plant caspase-like proteases in plant programmed cell death. Plant Signal Behav 4: 902-904.
    • (2009) Plant Signal Behav , vol.4 , pp. 902-904
    • Xu, Q.1    Zhang, L.2
  • 53
    • 85047684006 scopus 로고    scopus 로고
    • A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves
    • Yamada K, Matsushima R, Nishimura M, Hara-Nishimura I (2001) A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves. Plant Physiol 127: 1626-1634.
    • (2001) Plant Physiol , vol.127 , pp. 1626-1634
    • Yamada, K.1    Matsushima, R.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 54
    • 70450193165 scopus 로고    scopus 로고
    • The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for its formation and accumulates specific ß-glucosidases
    • Yamada K, Nagano AJ, Ogasawara K, Hara-Nishimura I, Nishimura M (2009) The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for its formation and accumulates specific ß-glucosidases. Plant Signal Behav 4: 849-852.
    • (2009) Plant Signal Behav , vol.4 , pp. 849-852
    • Yamada, K.1    Nagano, A.J.2    Ogasawara, K.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 55
    • 83255189504 scopus 로고    scopus 로고
    • Unique defense strategies by the endoplasmic reticulum body in plants
    • doi:10.1093/pcp/pcr156
    • Yamada K, Hara-Nishimura I, Nishimura M (2011) Unique defense strategies by the endoplasmic reticulum body in plants. Plant Cell Physiol 52: 2039-2049. doi: 10. 1093/pcp/pcr156.
    • (2011) Plant Cell Physiol , vol.52 , pp. 2039-2049
    • Yamada, K.1    Hara-Nishimura, I.2    Nishimura, M.3
  • 56
    • 84871814088 scopus 로고    scopus 로고
    • Identification of two novel endoplasmic reticulum body-specific integral membrane proteins
    • doi:10.1104/pp.112.207654
    • Yamada K, Nagano AJ, Nishina M, Hara-Nishimura I, Nishimura M (2013) Identification of two novel endoplasmic reticulum body-specific integral membrane proteins. Plant Physiol 161: 108-120. doi: 10. 1104/pp. 112. 207654.
    • (2013) Plant Physiol , vol.161 , pp. 108-120
    • Yamada, K.1    Nagano, A.J.2    Nishina, M.3    Hara-Nishimura, I.4    Nishimura, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.